The Function of SUMOylation and Its Role in the Development of Cancer Cells under Stress Conditions: A Systematic Review

Figure 1

The SUMOylation pathway. All SUMO paralogues are synthesized as preproteins which are first cleaved by sentrin-specific proteases (SENPs) and then exposed to the carboxy-terminal diglycine (GG) motif. By consuming an ATP for activation by E1 (SAE1-SAE2), resulting in formation of a SUMO E1 thioester complex. The formation of a SUMO E1 thioester complex can be blocked by ginkgolic acid, anacardic acid, and kerriamycin B. SUMO is transferred to SUMO E2 and linked to a thioester, which can be inhibited by spectomycin B1. SUMO can be directly transferred to the target protein by Ubc9, or sometimes SUMO E3 ligases are also required to connect SUMO to the target proteins at their lysine residues, which can be inhibited by 2-D08 and reversed by SENPs.